CAZyme Information: TSTA_044290-t26_1-p1

Basic Information

• Species: Talaromyces stipitatus
• Lineage: Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces stipitatus
• CAZyme ID: TSTA_044290-t26_1-p1
• CAZy Family: GH135
• CAZyme Description: glucoamylase precursor, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
616	EQ962657|CGC14	65365.52	4.1569

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TstipitatusATCC10500	12629	441959	146	12483

• Gene Location: location=EQ962657:1098344-1100417(+)

Full Sequence      

MAVTAVLAALNLLISVQGAVVESVPRASGSLDSWLAAETPIALQGVLNNIGSGGVFTEGA
VEGIVIASPSKADPNYYYTWTRDSALTLKTLVDNFIAGASDLESTIKDYINIESVLQGVS
NPSGSITDGSGLGEPKFNVDGTAFTGAWGRPQRDGPALRATAMIAYANYLIDNGQTSTAK
EIIWPIVQNDLAYVAQYWNQTTFDLWEETQGSSFFTTTAQHRALVEGNTLATALGESCAN
CVSQAPQILCFLQSYWTGSYILANFANNGRTGLDANSILGVIETFDPEASSCDDVTFQPC
SERALASHKAVTDSFRSIYSLNSGIAAGSAVAVGRYPEDVYQAGNPWYLATTAAAEQLYD
AIYQWNKIGFINITSISLSFFQAIYPSAATGTYAAGSSTFNALISAVKTYADGYMSVVER
YTPADGTLSEQFQRDNGVPLSASALTWSYAALLTAAARRAGTVPASWGSSKANTVPTTCS
ASSAKGSYTSATNTAWPTAPTSSTRPSCTPPSDVSVTFQEIVTTSPGQDIYLTGNISALG
SWSTTAGKAIALSAQDYRSADNLWYVALTLPSDTAFEYKFFKNESGMIIWEDDPNRVYVV
PSDCGVSTACINDSWQ

Enzyme Prediction     

EC	3.2.1.3:94	1.14.99.55:4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	59	456	1.2e-78	0.9501385041551247
CBM20	514	604	9.6e-24	0.9555555555555556

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	3.52e-137	40	449	1	409	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	5.99e-39	508	615	1	106	Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
395557	CBM_20	2.60e-30	514	609	1	94	Starch binding domain.
99883	CBM20_alpha_amylase	1.02e-24	514	615	1	94	Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
119437	CBM20	1.03e-21	515	615	1	96	The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
APM84499.1|CBM20|GH15	0.0	1	616	1	616
QGA19176.1|CBM20|GH15	0.0	1	616	1	616
QKX64217.1|CBM20|GH15	4.97e-314	5	616	6	613
CAC28076.1|CBM20|GH15|3.2.1.3	4.49e-297	26	616	27	618
ABH92242.1|CBM20|GH15|3.2.1.3	4.49e-297	26	616	27	618

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FRV_A	4.68e-244	30	616	2	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
6FHV_A	2.21e-219	29	616	6	593	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
2VN4_A	9.87e-217	30	616	1	598	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
3EQA_A	6.41e-215	30	497	2	467	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
1AGM_A	3.67e-214	30	497	2	466	Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. x100 to 2.4 angstroms resolution [Aspergillus awamori],1DOG_A REFINED STRUCTURE FOR THE COMPLEX OF 1-DEOXYNOJIRIMYCIN WITH GLUCOAMYLASE FROM (ASPERGILLUS AWAMORI) VAR. X100 TO 2.4 ANGSTROMS RESOLUTION [Aspergillus awamori],1GLM_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori],3GLY_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P69327|AMYG_ASPAW	5.60e-243	30	616	26	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P69328|AMYG_ASPNG	5.60e-243	30	616	26	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P22832|AMYG_ASPUS	7.66e-243	23	616	19	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P23176|AMYG_ASPKA	8.82e-242	30	616	26	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
sp|P36914|AMYG_ASPOR	1.49e-238	21	616	20	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000277	0.999704	CS pos: 18-19. Pr: 0.9814

TMHMM  Annotations     

There is no transmembrane helices in TSTA_044290-t26_1-p1.